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PDBsum entry 5da9
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433 a.a.
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400 a.a.
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85 a.a.
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60 a.a.
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PDB id:
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Hydrolase
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Title:
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Atp-gamma-s bound rad50 from chaetomium thermophilum in complex with the rad50-binding domain of mre11
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Structure:
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Putative uncharacterized protein,putative uncharacterized protein. Chain: a, b. Engineered: yes. Putative double-strand break protein. Chain: c, d. Engineered: yes
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Source:
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Chaetomium thermophilum var. Thermophilum dsm 1495. Organism_taxid: 759272. Gene: ctht_0073630. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ctht_0007600. Expression_system_taxid: 562
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Resolution:
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3.00Å
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R-factor:
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0.218
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R-free:
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0.258
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Authors:
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F.U.Seifert,K.Lammens,G.Stoehr,B.Kessler,K.-P.Hopfner
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Key ref:
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F.U.Seifert
et al.
(2016).
Structural mechanism of ATP-dependent DNA binding and DNA end bridging by eukaryotic Rad50.
Embo J,
35,
759-772.
PubMed id:
DOI:
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Date:
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19-Aug-15
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Release date:
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02-Mar-16
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PROCHECK
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Headers
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References
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G0SHW7
(G0SHW7_CHATD) -
DNA repair protein RAD50 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq:
Struc:
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1315 a.a.
433 a.a.*
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G0SHW7
(G0SHW7_CHATD) -
DNA repair protein RAD50 from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq:
Struc:
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1315 a.a.
400 a.a.*
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Enzyme class 2:
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Chains A, B:
E.C.3.6.-.-
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Enzyme class 3:
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Chains C, D:
E.C.3.1.-.-
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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DOI no:
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Embo J
35:759-772
(2016)
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PubMed id:
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Structural mechanism of ATP-dependent DNA binding and DNA end bridging by eukaryotic Rad50.
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F.U.Seifert,
K.Lammens,
G.Stoehr,
B.Kessler,
K.P.Hopfner.
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ABSTRACT
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The Mre11-Rad50-Nbs1 (MRN) complex is a central factor in the repair
ofDNAdouble-strand breaks (DSBs). TheATP-dependent mechanisms of howMRNdetects
and endonucleolytically processesDNAends for the repair by
microhomology-mediated end-joining or further resection in homologous
recombination are still unclear. Here, we report the crystal structures of
theATPγS-bound dimer of the Rad50(NBD)(nucleotide-binding domain) from the
thermophilic eukaryoteChaetomium thermophilum(Ct) in complex with
eitherDNAorCtMre11(RBD)(Rad50-binding domain) along with small-angle X-ray
scattering and cross-linking studies. The structure andDNAbinding motifs were
validated byDNAbinding experimentsin vitroand mutational analyses
inSaccharomyces cerevisiae in vivo Our analyses provide a structural framework
for the architecture of the eukaryotic Mre11-Rad50 complex. They show that a
Rad50 dimer binds approximately 18 base pairs ofDNAalong the dimer interface in
anATP-dependent fashion or bridges two DNAends with a preference for 3'
overhangs. Finally, our results may provide a general framework for the
interaction ofABC ATPase domains of the Rad50/SMC/RecN protein family with DNA.
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